2FAL

X-RAY CRYSTAL STRUCTURE OF FERRIC APLYSIA LIMACINA MYOGLOBIN IN DIFFERENT LIGANDED STATES

2FAL の概要

• エントリーDOI: 10.2210/pdb2fal/pdb
• 分子名称: MYOGLOBIN, CYANIDE ION, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• 機能のキーワード: oxygen storage
• 由来する生物種: Aplysia limacina (slug sea hare)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15991.94

構造登録者

Conti, E.,Moser, C.,Rizzi, M.,Mattevi, A.,Lionetti, C.,Coda, A.,Ascenzi, P.,Brunori, M.,Bolognesi, M. (登録日: 1993-06-14, 公開日: 1993-10-31, 最終更新日: 2024-10-30)

主引用文献

Conti, E.,Moser, C.,Rizzi, M.,Mattevi, A.,Lionetti, C.,Coda, A.,Ascenzi, P.,Brunori, M.,Bolognesi, M.
X-ray crystal structure of ferric Aplysia limacina myoglobin in different liganded states.
J.Mol.Biol., 233:498-508, 1993

PubMed Abstract: The X-ray crystal structure of the ligand-free ferric form of Aplysia limacina myoglobin (pH 6.0) has been refined at 1.7 A resolution (R = 15.1%), and its cyanide, thiocyanate and imidazole derivatives studied by difference Fourier techniques at atomic resolution. The crystallographic R-factors of the three different derivatives reported are 16.1%, 16.1% and 15.6% at 1.8 A, 2.0 A and 2.0 A resolution, respectively. The present results have been analyzed in parallel with previous crystallographic studies on the molecular structures of the fluoride and azide derivatives of ferric Aplysia limacina myoglobin. Ligand binding to the distal site of the heme pocket results in different networks of hydrogen bonds involving to various degrees the bound ligand, residue Arg(66)E10, the heme propionate III, ordered water molecules and/or protein backbone atoms from the CD region. In particular, Arg(66)E10 stabilizes the bound ligand and compensates for the absence of the hydrogen bond donor residue HisE7, commonly present in oxygen-carrying globins.

PubMed: 8411158
DOI: 10.1006/jmbi.1993.1527

実験手法

X-RAY DIFFRACTION (1.8 Å)